Preliminary X-ray crystallographic studies of the Mycobacterium Tuberculosis HSP16.3 molecular chaperone

被引:2
作者
Chen, Y
An, J
Ding, Y
Dai, H
Mao, Q
Feng, L
Liu, B
Chang, Y
Chen, F
He, H
Tang, H
Chang, Z
Rao, Z
机构
[1] Tsinghua Univ, Struct Biol Lab, Beijing 100084, Peoples R China
[2] Tsinghua Univ, Prot Sci Lab, MOE, Beijing 100084, Peoples R China
关键词
Mycobacterium Tuberculosis HSP16.3; molecular chaperone; small heat shock protein (sHSP); crystallization;
D O I
10.2174/0929866013409111
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Mycobacterium Tuberculosis HSP16.3 is a major antigen maximally expressed during the stationary phase. Previous studies showed that HSP16.3 can function as a molecular chaperone in vitro. Here, crystallization trails of HSP 16.3 were reported. A kind of crystal can be diffracted to 2.8 Angstrom resolution at the "Photon Factory", a synchrotron light source in Japan. The crystal displayed the space group R3 with unit cell parameters a=b=110 Angstrom, c=152 Angstrom and Y=120 degrees. Assuming the presence of 9 HSP16.3 molecules in an asymmetric unit, it gives a Vm= 0.73 Angstrom (3)/Da. and solvent content of 35% by volume.
引用
收藏
页码:499 / 502
页数:4
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